Unique Substrate Specificity of SplE Serine Protease from Staphylococcus aureus.
Structure
; 26(4): 572-579.e4, 2018 04 03.
Article
em En
| MEDLINE
| ID: mdl-29526434
ABSTRACT
Staphylococcus aureus is a dangerous human pathogen characterized by alarmingly increasing antibiotic resistance. Accumulating evidence suggests the role of Spl proteases in staphylococcal virulence. Spl proteases have restricted, non-overlapping substrate specificity, suggesting that they may constitute a first example of a proteolytic system in bacteria. SplA, SplB, and SplD were previously characterized in terms of substrate specificity and structural determinants thereof. Here we analyze the substrate specificity of SplE documenting its unique P1 preference among Spl proteases and, in fact, among all chymotrypsin-like (family S1) proteases characterized to date. This is interesting since our understanding of the general aspects of proteolysis is based on seminal studies of S1 family members. To better understand the molecular determinants of the unusual specificity of SplE, the crystal structure of the protein is determined here. Conclusions from structural analysis are evaluated by successful grafting of SplE specificity on the scaffold of SplB protease.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Contexto em Saúde:
3_ND
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Staphylococcus aureus
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Proteínas de Bactérias
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Fatores de Virulência
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Serina Proteases
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Structure
Ano de publicação:
2018
Tipo de documento:
Article